1gmw
From Proteopedia
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| - | [[Image:1gmw.gif|left|200px]] | + | [[Image:1gmw.gif|left|200px]] |
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| - | '''STRUCTURE OF UREE''' | + | {{Structure |
| + | |PDB= 1gmw |SIZE=350|CAPTION= <scene name='initialview01'>1gmw</scene>, resolution 1.5Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+D'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF UREE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GMW is a [ | + | 1GMW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMW OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation., Song HK, Mulrooney SB, Huber R, Hausinger RP, J Biol Chem. 2001 Dec 28;276(52):49359-64. Epub 2001 Oct 8. PMID:[http:// | + | Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation., Song HK, Mulrooney SB, Huber R, Hausinger RP, J Biol Chem. 2001 Dec 28;276(52):49359-64. Epub 2001 Oct 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11591723 11591723] |
[[Category: Klebsiella aerogenes]] | [[Category: Klebsiella aerogenes]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: metallochaperone]] | [[Category: metallochaperone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:25:12 2008'' |
Revision as of 09:25, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF UREE
Overview
UreE is proposed to be a metallochaperone that delivers nickel ions to urease during activation of this bacterial virulence factor. Wild-type Klebsiella aerogenes UreE binds approximately six nickel ions per homodimer, whereas H144*UreE (a functional C-terminal truncated variant) was previously reported to bind two. We determined the structure of H144*UreE by multi-wavelength anomalous diffraction and refined it to 1.5 A resolution. The present structure reveals an Hsp40-like peptide-binding domain, an Atx1-like metal-binding domain, and a flexible C terminus. Three metal-binding sites per dimer, defined by structural analysis of Cu-H144*UreE, are on the opposite face of the Atx1-like domain than observed in the copper metallochaperone. One metal bridges the two subunits via the pair of His-96 residues, whereas the other two sites involve metal coordination by His-110 and His-112 within each subunit. In contrast to the copper metallochaperone mechanism involving thiol ligand exchanges between structurally similar chaperones and target proteins, we propose that the Hsp40-like module interacts with urease apoprotein and/or other urease accessory proteins, while the Atx1-like domain delivers histidyl-bound nickel to the urease active site.
About this Structure
1GMW is a Protein complex structure of sequences from Klebsiella aerogenes. Full crystallographic information is available from OCA.
Reference
Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation., Song HK, Mulrooney SB, Huber R, Hausinger RP, J Biol Chem. 2001 Dec 28;276(52):49359-64. Epub 2001 Oct 8. PMID:11591723
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